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Database: UniProt
Entry: C7BKK1_PHOAA
LinkDB: C7BKK1_PHOAA
Original site: C7BKK1_PHOAA 
ID   C7BKK1_PHOAA            Unreviewed;       415 AA.
AC   C7BKK1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   Name=amiC {ECO:0000313|EMBL:CAQ82687.1};
GN   OrderedLocusNames=PAU_00595 {ECO:0000313|EMBL:CAQ82687.1};
OS   Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS   (Xenorhabdus luminescens (strain 2)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ82687.1, ECO:0000313|Proteomes:UP000002747};
RN   [1] {ECO:0000313|EMBL:CAQ82687.1, ECO:0000313|Proteomes:UP000002747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747};
RX   PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA   Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA   Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA   Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA   Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT   "Comparative genomics of the emerging human pathogen Photorhabdus
RT   asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL   BMC Genomics 10:302-302(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001561};
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DR   EMBL; FM162591; CAQ82687.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7BKK1; -.
DR   STRING; 291112.PAU_00595; -.
DR   KEGG; pay:PAU_00595; -.
DR   eggNOG; COG0860; Bacteria.
DR   Proteomes; UP000002747; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3500; -; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   NCBIfam; NF038267; amidase_AmiC; 1.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF11741; AMIN; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CAQ82687.1}.
FT   DOMAIN          249..403
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   415 AA;  46376 MW;  66B2FDFB03B31B94 CRC64;
     MSHSDHNLSR RRLLQGAAAM WLLSVSHVGY ASSSKIIAVR IWPASSYTRV TLESNIPLKY
     RQFMLTNPNR IVVDLEGVQL NHTLKGMGEQ IQSRDPYLKL VRAGQFDPKT VRLVFEVKQP
     VSPHMFTLKP VAEFKHRLVL DLYPAAGTNT DDDPLLALLE EYNKGNLAED LPAKTPKPGK
     AGKDRPIVIM LDPGHGGEDP GAIGKYKTRE KDVVLQIARR LKSIIQREPD MKVYMTRNED
     VFIPLKVRVA KARKMRADLF VSIHADAFTN RAARGSSVFA LSTKGATSNT ARFLAQTQNE
     ADQIGGVSKS GDKYLDHTMF DLLQTATIND SLKFGSEVLR RMGKVNKLHK NRVDQAGFAV
     LKAPDIPSIL VETAFISNLE EERKLKTARF QQQVAESIFA GIKAYFRNGG DLVRR
//
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